Scholarlink

Abstract <p>The effect of the C-terminal tail on the bioactivity of <i>Agaricus bisporus</i> mannose-binding protein (Abmb) was investigated. Based on the earlier obtained crystal structure of Abmb, it was suggested that the additional C-terminal tail can modulate the binding of sugars to the protein. According to glycan microarray, Abmb can bind β-Gal sugars, which contradicted the results of SPR analysis showing that Abmb only interacts with α-Man and not with α-Gal. Here, we used MCF-7 and MDA-MB-231 breast cancer cells to demonstrate that the presence of the C-terminal tail decreased the anti-proliferative activity of Abmb. Pre-incubating Abmb with α-Gal did not eliminate the anti-proliferative activity, while pre-incubation with α-Man attenuated it. At&#xa0;the same time, preincubation with a mixture of α-Gal and α-Man strongly promoted the anti-proliferative activity of Abmb. <i>In&#xa0;silico</i> analysis using molecular docking suggested the presence of a second functional sugar-binding site for Gal, which had not been identified previously. The study provides new insights into the structure of lectins and their interaction with sugars</p>

错误：搜索内容不能为空，请输入英文关键词
错误：关键词超出字数限制，请精简
高级检索

Unraveling the Effect of the C-terminal Tail of Agaricus bisporus Mannose-Binding Protein and Discovery of a Second Functional Sugar-Binding Site

  • 期刊论文

  • 发表日期：

    2025年10月31日

查看全文
  • Anis P. Rahayu,
  • Zunia R. Akhwan,
  • Agung H. Karsono,
  • Hiromi Yoshida,
  • Ratna A. Utami,
  • Raymond R. Tjandrawinata,
  • Heni Rachmawati,
  • Wangsa T. Ismaya

摘要

Abstract

The effect of the C-terminal tail on the bioactivity of Agaricus bisporus mannose-binding protein (Abmb) was investigated. Based on the earlier obtained crystal structure of Abmb, it was suggested that the additional C-terminal tail can modulate the binding of sugars to the protein. According to glycan microarray, Abmb can bind β-Gal sugars, which contradicted the results of SPR analysis showing that Abmb only interacts with α-Man and not with α-Gal. Here, we used MCF-7 and MDA-MB-231 breast cancer cells to demonstrate that the presence of the C-terminal tail decreased the anti-proliferative activity of Abmb. Pre-incubating Abmb with α-Gal did not eliminate the anti-proliferative activity, while pre-incubation with α-Man attenuated it. At the same time, preincubation with a mixture of α-Gal and α-Man strongly promoted the anti-proliferative activity of Abmb. In silico analysis using molecular docking suggested the presence of a second functional sugar-binding site for Gal, which had not been identified previously. The study provides new insights into the structure of lectins and their interaction with sugars